Similarities and differences between human cyclophilin A and other beta-barrel structures. Structural refinement at 1.63 A resolution.

@article{Ke1992SimilaritiesAD,
  title={Similarities and differences between human cyclophilin A and other beta-barrel structures. Structural refinement at 1.63 A resolution.},
  author={Hengming Ke},
  journal={Journal of molecular biology},
  year={1992},
  volume={228 2},
  pages={539-50}
}
  • Hengming Ke
  • Published 1992 in Journal of molecular biology
The structure of the unligated recombinant human cyclophilin A (CyP A) has been refined to an R-factor of 0.18 at 1.63 A resolution. The root-mean-squared deviations of the refined structure are 0.013 A and 2.50 degrees from ideal geometries of bond length and bond angle, respectively. Eight antiparallel beta-strands of CyP A form a right-handed beta-barrel. The structure of CyP A is compared with other members in the antiparallel eight-stranded beta-barrel family and with the parallel eight… CONTINUE READING